Expression and purification of Src I from sea anemone Sagartia rosea as a recombinant non-fusion protein
Related Experiment Video
Updated: Aug 29, 2026
Recombinant Protein Expression for Structural Biology in HEK 293F Suspension Cells: A Novel and Accessible Approach
Published on: October 16, 2014
Xiaoyu Jiang1, Lisheng Peng, Wenli Yang
1The Open Laboratory for Marine Functional Genomics of State High-Tech Development, Department of Biochemistry, College of Life Sciences, Sun Yat-sen (Zhongshan) University, Guangzhou 510275, People's Republic of China.
Abstract:
The cDNA coding for an acidic actinoporin, Sagartia rosea cytolysin I (Src I), has been isolated, cloned into pGEM-T Easy Vector, and sequenced. The region encoding matured Src I was also cloned into prokaryotic expression vector pBV220 and expressed in Escherichia coli as a non-fusion protein in the form of inclusion body. Through washing and denaturation-renaturation step, the recombinant Src I was purified by Q Sepharose Fast Flow ion exchange chromatography and Phenyl Sepharose hydrophobic interaction chromatography. The two-step purification of Src I was effective, simple, and suitable for isolating large amount of high purity (above 95%) recombinant Src I.
More Related Videos
12:16High Throughput Quantitative Expression Screening and Purification Applied to Recombinant Disulfide-rich Venom Proteins Produced in E. coli
Published on: July 30, 2014
11:42High Yield Expression of Recombinant Human Proteins with the Transient Transfection of HEK293 Cells in Suspension
Published on: December 28, 2015
